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      CD1d-lipid-antigen recognition by the semi-invariant NKT T-cell receptor.

      Nature

      Animals, Antigen Presentation, Antigens, CD1, chemistry, immunology, Antigens, CD1d, Carbohydrate Conformation, Crystallography, X-Ray, Galactosylceramides, Humans, Killer Cells, Natural, Mice, Protein Conformation, Receptors, Antigen, T-Cell, alpha-beta, Species Specificity, T-Lymphocyte Subsets, T-Lymphocytes

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          Abstract

          The CD1 family is a large cluster of non-polymorphic, major histocompatibility complex (MHC) class-I-like molecules that bind distinct lipid-based antigens that are recognized by T cells. The most studied group of T cells that interact with lipid antigens are natural killer T (NKT) cells, which characteristically express a semi-invariant T-cell receptor (NKT TCR) that specifically recognizes the CD1 family member, CD1d. NKT-cell-mediated recognition of the CD1d-antigen complex has been implicated in microbial immunity, tumour immunity, autoimmunity and allergy. Here we describe the structure of a human NKT TCR in complex with CD1d bound to the potent NKT-cell agonist alpha-galactosylceramide, the archetypal CD1d-restricted glycolipid. In contrast to T-cell receptor-peptide-antigen-MHC complexes, the NKT TCR docked parallel to, and at the extreme end of the CD1d-binding cleft, which enables a lock-and-key type interaction with the lipid antigen. The structure provides a basis for the interaction between the highly conserved NKT TCR alpha-chain and the CD1d-antigen complex that is typified in innate immunity, and also indicates how variability of the NKT TCR beta-chain can impact on recognition of other CD1d-antigen complexes. These findings provide direct insight into how a T-cell receptor recognizes a lipid-antigen-presenting molecule of the immune system.

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          Journal
          17581592
          10.1038/nature05907

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